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Published on: February 12, 2016
Transglutaminase-enhanced walnut protein isolate gels: Synergistic effects of double modification on gelation and
Mengxin Wang1, Rui Chen1, Long Wu1
1State Key Laboratory of Efficient Production of Forest Resources, Beijing Key Laboratory of Forestry Food Processing and Safety, School of Biological Sciences and Technology, Beijing Forestry University, Beijing, China.
Abstract:
This study investigated the effects of a double-modification process involving Alcalase hydrolysis (1, 3, and 5 min) and ultrasound treatment (360 W, 15 min) on the functional properties and characteristics of walnut protein isolate (WPI). Among the treatments, WPI hydrolyzed for 3 min and subjected to ultrasound (WEU-3) demonstrated the highest water-holding capacity of 3.66 g/g and solubility of 34.68 %. Gels were subsequently prepared using transglutaminase (TG) to cross-link WEU-5, which served as a carrier for riboflavin. Scanning electron microscopy revealed a compact and homogeneous network structure in the gels. Low-field nuclear magnetic resonance analysis indicated that TG cross-linking facilitated the migration of bound water into the gel network, enhancing its rheological properties. During simulated gastrointestinal digestion, the sample treated with 30 U/g of TG showed the lowest riboflavin release (73.02 %) after 360 min. These findings suggest that the double-modification process combined with TG treatment improves the gelling properties and nutrient delivery potential of WPI.

